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Magnesium in PDB 6r4p: Structure of A Soluble Domain of Adenylyl Cyclase Bound to An Activated Stimulatory G Protein

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of A Soluble Domain of Adenylyl Cyclase Bound to An Activated Stimulatory G Protein (pdb code 6r4p). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of A Soluble Domain of Adenylyl Cyclase Bound to An Activated Stimulatory G Protein, PDB code: 6r4p:

Magnesium binding site 1 out of 1 in 6r4p

Go back to Magnesium Binding Sites List in 6r4p
Magnesium binding site 1 out of 1 in the Structure of A Soluble Domain of Adenylyl Cyclase Bound to An Activated Stimulatory G Protein


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of A Soluble Domain of Adenylyl Cyclase Bound to An Activated Stimulatory G Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg502

b:72.0
occ:1.00
O2B B:GSP501 2.1 76.3 1.0
OG B:SER54 2.1 70.9 1.0
O2G B:GSP501 2.1 76.3 1.0
OG1 B:THR204 2.1 75.0 1.0
CB B:THR204 2.8 75.0 1.0
CB B:SER54 3.2 70.9 1.0
PB B:GSP501 3.3 76.3 1.0
PG B:GSP501 3.5 76.3 1.0
CG2 B:THR204 3.7 75.0 1.0
O3B B:GSP501 3.7 76.3 1.0
N B:SER54 3.9 70.9 1.0
OD1 B:ASP223 3.9 69.1 1.0
N B:THR204 3.9 75.0 1.0
CA B:THR204 3.9 75.0 1.0
O1B B:GSP501 3.9 76.3 1.0
CA B:SER54 4.1 70.9 1.0
OD2 B:ASP223 4.1 69.1 1.0
NZ B:LYS53 4.3 65.6 1.0
O2A B:GSP501 4.3 76.3 1.0
O B:VAL224 4.4 66.1 1.0
O3G B:GSP501 4.4 76.3 1.0
CG B:ASP223 4.4 69.1 1.0
O B:VAL202 4.5 79.6 1.0
O3A B:GSP501 4.6 76.3 1.0
S1G B:GSP501 4.6 76.3 1.0
CB B:LYS53 4.7 65.6 1.0
PA B:GSP501 4.8 76.3 1.0
CA B:GLY225 4.9 69.3 1.0
O1A B:GSP501 4.9 76.3 1.0
C B:LYS53 4.9 65.6 1.0
C B:THR204 5.0 75.0 1.0

Reference:

C.Qi, S.Sorrentino, O.Medalia, V.M.Korkhov. The Structure of A Membrane Adenylyl Cyclase Bound to An Activated Stimulatory G Protein. Science V. 364 389 2019.
ISSN: ESSN 1095-9203
PubMed: 31023924
DOI: 10.1126/SCIENCE.AAV0778
Page generated: Tue Oct 1 16:34:21 2024

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